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P20020 (AT2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plasma membrane calcium-transporting ATPase 1

Short name=PMCA1
EC=3.6.3.8
Alternative name(s):
Plasma membrane calcium ATPase isoform 1
Plasma membrane calcium pump isoform 1
Gene names
Name:ATP2B1
Synonyms:PMCA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell.

Catalytic activity

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Subunit structure

Interacts with PDZD11. Ref.12

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Isoform B is ubiquitously expressed. Isoform C is found in brain cortex, skeletal muscle and heart muscle. Isoform D has only been found in fetal skeletal muscle. Isoform K has been found in small intestine and liver.

Domain

The calmodulin-binding subdomain B is different in the different splice variants and shows pH dependent calmodulin binding properties in isoforms A, C, D and E.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIB subfamily. [View classification]

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform D (identifier: P20020-1)

Also known as: CIV;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A (identifier: P20020-2)

Also known as: CII;

The sequence of this isoform differs from the canonical sequence as follows:
     1156-1258: IRVVNAFRSS...SPLHSLETSL → VVFSSSTASTTVGYSSGECIS
Isoform B (identifier: P20020-3)

Also known as: CI;

The sequence of this isoform differs from the canonical sequence as follows:
     1118-1155: Missing.
Isoform C (identifier: P20020-4)

Also known as: CIII;

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1155: Missing.
Isoform E (identifier: P20020-5)

Also known as: CV;

The sequence of this isoform differs from the canonical sequence as follows:
     1156-1258: IRVVNAFRSS...SPLHSLETSL → VVFSSSTASTTVGFEW
Isoform K (identifier: P20020-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1021-1056: Missing.
     1118-1155: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 12581257Plasma membrane calcium-transporting ATPase 1
PRO_0000046209

Regions

Topological domain2 – 9796Cytoplasmic Potential
Transmembrane98 – 11821Helical; Potential
Topological domain119 – 15436Extracellular Potential
Transmembrane155 – 17521Helical; Potential
Topological domain176 – 366191Cytoplasmic Potential
Transmembrane367 – 38620Helical; Potential
Topological domain387 – 41933Extracellular Potential
Transmembrane420 – 43718Helical; Potential
Topological domain438 – 852415Cytoplasmic Potential
Transmembrane853 – 87220Helical; Potential
Topological domain873 – 88210Extracellular Potential
Transmembrane883 – 90321Helical; Potential
Topological domain904 – 92320Cytoplasmic Potential
Transmembrane924 – 94623Helical; Potential
Topological domain947 – 96418Extracellular Potential
Transmembrane965 – 98622Helical; Potential
Topological domain987 – 100519Cytoplasmic Potential
Transmembrane1006 – 102722Helical; Potential
Topological domain1028 – 103710Extracellular Potential
Transmembrane1038 – 105922Helical; Potential
Topological domain1060 – 1258199Cytoplasmic Potential
Region1100 – 111718Calmodulin-binding subdomain A
Region1118 – 112710Calmodulin-binding subdomain B
Compositional bias296 – 2994Poly-Glu

Sites

Active site47514-aspartylphosphate intermediate
Metal binding7971Magnesium By similarity
Metal binding8011Magnesium By similarity

Amino acid modifications

Modified residue21N-acetylglycine Ref.15
Modified residue171Phosphoserine Ref.14
Modified residue11161Phosphothreonine; by PKC
Modified residue11931Phosphoserine Ref.13 Ref.14 Ref.15 Ref.17
Modified residue12031Phosphothreonine Ref.14 Ref.15
Modified residue12161Phosphoserine; by PKA Ref.14 Ref.17
Modified residue12201Phosphoserine Ref.13 Ref.14 Ref.17

Natural variations

Alternative sequence1021 – 105636Missing in isoform K.
VSP_000372
Alternative sequence1118 – 115538Missing in isoform B and isoform K.
VSP_000373
Alternative sequence1147 – 11559Missing in isoform C.
VSP_000374
Alternative sequence1156 – 1258103IRVVN…LETSL → VVFSSSTASTTVGYSSGECI S in isoform A.
VSP_000375
Alternative sequence1156 – 1258103IRVVN…LETSL → VVFSSSTASTTVGFEW in isoform E.
VSP_000376
Natural variant2671M → R Rare polymorphism. Ref.18
VAR_000698

Experimental info

Sequence conflict259 – 2624LLLS → MSAT in AAA36000. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform D (CIV) [UniParc].

Last modified June 1, 2001. Version 3.
Checksum: 7037112747FC9B0A

FASTA1,258138,755
        10         20         30         40         50         60 
MGDMANNSVA YSGVKNSLKE ANHDGDFGIT LAELRALMEL RSTDALRKIQ ESYGDVYGIC 

        70         80         90        100        110        120 
TKLKTSPNEG LSGNPADLER REAVFGKNFI PPKKPKTFLQ LVWEALQDVT LIILEIAAIV 

       130        140        150        160        170        180 
SLGLSFYQPP EGDNALCGEV SVGEEEGEGE TGWIEGAAIL LSVVCVVLVT AFNDWSKEKQ 

       190        200        210        220        230        240 
FRGLQSRIEQ EQKFTVIRGG QVIQIPVADI TVGDIAQVKY GDLLPADGIL IQGNDLKIDE 

       250        260        270        280        290        300 
SSLTGESDHV KKSLDKDPLL LSGTHVMEGS GRMVVTAVGV NSQTGIIFTL LGAGGEEEEK 

       310        320        330        340        350        360 
KDEKKKEKKN KKQDGAIENR NKAKAQDGAA MEMQPLKSEE GGDGDEKDKK KANLPKKEKS 

       370        380        390        400        410        420 
VLQGKLTKLA VQIGKAGLLM SAITVIILVL YFVIDTFWVQ KRPWLAECTP IYIQYFVKFF 

       430        440        450        460        470        480 
IIGVTVLVVA VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL 

       490        500        510        520        530        540 
TMNRMTVVQA YINEKHYKKV PEPEAIPPNI LSYLVTGISV NCAYTSKILP PEKEGGLPRH 

       550        560        570        580        590        600 
VGNKTECALL GLLLDLKRDY QDVRNEIPEE ALYKVYTFNS VRKSMSTVLK NSDGSYRIFS 

       610        620        630        640        650        660 
KGASEIILKK CFKILSANGE AKVFRPRDRD DIVKTVIEPM ASEGLRTICL AFRDFPAGEP 

       670        680        690        700        710        720 
EPEWDNENDI VTGLTCIAVV GIEDPVRPEV PDAIKKCQRA GITVRMVTGD NINTARAIAT 

       730        740        750        760        770        780 
KCGILHPGED FLCLEGKDFN RRIRNEKGEI EQERIDKIWP KLRVLARSSP TDKHTLVKGI 

       790        800        810        820        830        840 
IDSTVSDQRQ VVAVTGDGTN DGPALKKADV GFAMGIAGTD VAKEASDIIL TDDNFTSIVK 

       850        860        870        880        890        900 
AVMWGRNVYD SISKFLQFQL TVNVVAVIVA FTGACITQDS PLKAVQMLWV NLIMDTLASL 

       910        920        930        940        950        960 
ALATEPPTES LLLRKPYGRN KPLISRTMMK NILGHAFYQL VVVFTLLFAG EKFFDIDSGR 

       970        980        990       1000       1010       1020 
NAPLHAPPSE HYTIVFNTFV LMQLFNEINA RKIHGERNVF EGIFNNAIFC TIVLGTFVVQ 

      1030       1040       1050       1060       1070       1080 
IIIVQFGGKP FSCSELSIEQ WLWSIFLGMG TLLWGQLIST IPTSRLKFLK EAGHGTQKEE 

      1090       1100       1110       1120       1130       1140 
IPEEELAEDV EEIDHAEREL RRGQILWFRG LNRIQTQMDV VNAFQSGSSI QGALRRQPSI 

      1150       1160       1170       1180       1190       1200 
ASQHHDVTNI STPTHIRVVN AFRSSLYEGL EKPESRSSIH NFMTHPEFRI EDSEPHIPLI 

      1210       1220       1230       1240       1250 
DDTDAEDDAP TKRNSSPPPS PNKNNNAVDS GIHLTIEMNK SATSSSPGSP LHSLETSL 

« Hide

Isoform A (CII) [UniParc].

Checksum: 5672202C16491703
Show »

FASTA1,176129,516
Isoform B (CI) [UniParc].

Checksum: 7E75C19B1A501423
Show »

FASTA1,220134,685
Isoform C (CIII) [UniParc].

Checksum: 8F56F132BE096587
Show »

FASTA1,249137,804
Isoform E (CV) [UniParc].

Checksum: 9FC9B1AA3B32B384
Show »

FASTA1,171129,152
Isoform K [UniParc].

Checksum: B1FB3E7116D2FDA2
Show »

FASTA1,184130,617

References

« Hide 'large scale' references
[1]"Complete primary structure of a human plasma membrane Ca2+ pump."
Verma A.K., Filoteo A.G., Stanford D.R., Wieben E.D., Penniston J.T., Strehler E.E., Fischer R., Heim R., Vogel G., Mathews S., Strehler-Page M.-A., James P., Vorherr T.E., Krebs J., Carafoli E.
J. Biol. Chem. 263:14152-14159(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Tissue: Erythrocyte.
[2]"Molecular cloning of a plasma membrane calcium pump from human osteoblasts."
Kumar R., Haugen J.D., Penniston J.T.
J. Bone Miner. Res. 8:505-513(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Tissue: Osteoblast.
[3]"Structure of the gene encoding the human plasma membrane calcium pump isoform 1."
Hilfiker H., Strehler-Page M.-A., Stauffer T.P., Carafoli E., Strehler E.E.
J. Biol. Chem. 268:19717-19725(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
Tissue: Leukocyte.
[4]Strehler E.E., Strehler-Page M.-A.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]"mRNAs for plasma membrane calcium pump isoforms differing in their regulatory domain are generated by alternative splicing that involves two internal donor sites in a single exon."
Strehler E.E., Strehler-Page M.-A., Vogel G., Carafoli E.
Proc. Natl. Acad. Sci. U.S.A. 86:6908-6912(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A; C AND D).
Tissue: Fetal skeletal muscle.
[6]"Study of calmodulin binding to the alternatively spliced C-terminal domain of the plasma membrane Ca2+ pump."
Kessler F., Falchetto R., Heim R., Meili R., Vorherr T.E., Strehler E.E., Carafoli E.
Biochemistry 31:11785-11792(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Fetal brain.
[7]"Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes."
Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.
J. Biol. Chem. 268:25993-26003(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND E).
Tissue: Brain cortex.
[8]Erratum
Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.
J. Biol. Chem. 269:32022-32022(1994) [PubMed] [Europe PMC] [Abstract]
[9]"Human and rat intestinal plasma membrane calcium pump isoforms."
Howard A., Legon S., Walters J.R.
Am. J. Physiol. 265:G917-G925(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM K).
Tissue: Small intestine mucosa.
[10]"Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump."
James P.H., Pruschy M., Vorherr T.E., Penniston J.T., Carafoli E.
Biochemistry 28:4253-4258(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CAMP KINASE.
[11]"Protein kinase C phosphorylates the carboxyl terminus of the plasma membrane Ca(2+)-ATPase from human erythrocytes."
Wang K.K.W., Wright L.C., Machan C.L., Allen B.G., Conigrave A.D., Roufogalis B.D.
J. Biol. Chem. 266:9078-9085(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PROTEIN KINASE C.
[12]"Characterization of PISP, a novel single-PDZ protein that binds to all plasma membrane Ca2+-ATPase b-splice variants."
Goellner G.M., DeMarco S.J., Strehler E.E.
Ann. N. Y. Acad. Sci. 986:461-471(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDZD11.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1193 AND SER-1220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-1193; THR-1203; SER-1216 AND SER-1220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1193 AND THR-1203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1193; SER-1216 AND SER-1220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Investigation of the Met-267 Arg exchange in isoform 1 of the human plasma membrane calcium pump in patients with essential hypertension by the amplification-created restriction site technique."
Benkwitz C., Kubsisch C., Kraft K., Neyses L.
J. Mol. Med. 75:62-66(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-267.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04027 mRNA. Translation: AAA74511.1.
M95541 mRNA. Translation: AAA35999.1.
M95542 mRNA. Translation: AAA36000.1.
L14561 Genomic DNA. Translation: AAD09924.1.
L14561 Genomic DNA. Translation: AAD09925.1.
M25824 Genomic DNA. Translation: AAA58383.1.
M25824 Genomic DNA. Translation: AAA58382.1.
M25824 Genomic DNA. Translation: AAA58381.1.
S49852 mRNA. Translation: AAB24324.1.
U15686 mRNA. Translation: AAA60983.1.
U15687 mRNA. Translation: AAA60984.1.
PIRA30802.
E49570.
I55491.
I70165.
RefSeqNP_001001323.1. NM_001001323.1.
NP_001673.2. NM_001682.2.
XP_005268976.1. XM_005268919.1.
UniGeneHs.506276.

3D structure databases

ProteinModelPortalP20020.
SMRP20020. Positions 66-946, 1100-1126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106980. 7 interactions.
IntActP20020. 4 interactions.
MINTMINT-5004114.
STRING9606.ENSP00000261173.

Protein family/group databases

TCDB3.A.3.2.25. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteP20020.

Polymorphism databases

DMDM14286104.

Proteomic databases

PaxDbP20020.
PRIDEP20020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261173; ENSP00000261173; ENSG00000070961. [P20020-3]
ENST00000348959; ENSP00000343599; ENSG00000070961. [P20020-6]
ENST00000359142; ENSP00000352054; ENSG00000070961. [P20020-2]
ENST00000428670; ENSP00000392043; ENSG00000070961. [P20020-3]
GeneID490.
KEGGhsa:490.
UCSCuc001tbf.3. human. [P20020-6]
uc001tbg.3. human. [P20020-2]
uc001tbh.3. human. [P20020-3]

Organism-specific databases

CTD490.
GeneCardsGC12M089981.
HGNCHGNC:814. ATP2B1.
HPACAB005605.
HPA011166.
HPA012945.
MIM108731. gene.
neXtProtNX_P20020.
PharmGKBPA25107.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOVERGENHBG061286.
KOK05850.
OMASESVMND.
OrthoDBEOG7SN8BN.
PhylomeDBP20020.
TreeFamTF300330.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP20020.
BgeeP20020.
CleanExHS_ATP2B1.
GenevestigatorP20020.

Family and domain databases

Gene3D1.20.1110.10. 1 hit.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProIPR022141. ATP_Ca_trans_C.
IPR006408. ATPase_P-typ_Ca-transp_plasma.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF12424. ATP_Ca_trans_C. 2 hits.
PF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01517. ATPase-IIB_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATP2B1.
GenomeRNAi490.
NextBio2053.
PROP20020.
SOURCESearch...

Entry information

Entry nameAT2B1_HUMAN
AccessionPrimary (citable) accession number: P20020
Secondary accession number(s): Q12992 expand/collapse secondary AC list , Q12993, Q13819, Q13820, Q13821, Q16504, Q93082
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM